EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   2.6.1.88 | 2-oxo-4-methylthiobutanoate + an L-amino acid |
a wide range of L-amino acids are effective donors, with Asp, Glu, Phe, His, Ile, Leu, Asn, Gln, Trp, and Tyr all producing more than 0.5 nM of L-methionine/min/mg of protein. Glu, Phe, Trp, and Tyr are the preferred amino donors, catalyzing the formation of above 1100 nM L-methionine/min/mg of protein |
Klebsiella pneumoniae |
L-methionine + a 2-oxo acid |
- |
? |
| 2.6.1.88 | 2-oxo-4-methylthiobutanoate + an L-amino acid |
isoleucine, leucine, and valine are the most effective substrates while glutamate and phenylalanine are also active as amino donors. Tyrosine and tryptophan have a much lesser ability to transaminate 2-oxo-4-methylthiobutanoate and all other L-amino acids are inactive |
Mycobacterium tuberculosis |
L-methionine + a 2-oxo acid |
- |
? |
| 2.6.1.88 | 2-oxo-4-methylthiobutanoate + an L-amino acid |
recombinant enzyme shows high activity with 2-oxo-4-methylthiobutanoate (100% activity at 0.1 and 2 mM) |
Arabidopsis thaliana |
L-methionine + a 2-oxo acid |
- |
r |
| 2.6.1.88 | 2-oxo-4-methylthiobutanoate + an L-amino acid |
a wide range of L-amino acids are effective donors, with Asp, Glu, Phe, His, Ile, Leu, Asn, Gln, Trp, and Tyr all producing more than 0.5 nM of L-methionine/min/mg of protein. Glu, Phe, Trp, and Tyr are the preferred amino donors, catalyzing the formation of above 1100 nM L-methionine/min/mg of protein |
Klebsiella pneumoniae ATCC 13883 |
L-methionine + a 2-oxo acid |
- |
? |
| 2.6.1.88 | 2-oxo-4-methylthiobutanoate + L-glutamate |
while L-glutamate is capable of producing the highest maximum initial velocity for L-methionine production from 2-oxo-4-methylthiobutanoate, it is 5-10fold poorer in terms of substrate specificity when compared with L-tyrosine, L-tryptophan, and L-phenylalanine |
Klebsiella pneumoniae |
L-methionine + 2-oxoglutarate |
- |
? |
| 2.6.1.88 | 2-oxo-4-methylthiobutanoate + L-glutamate |
while L-glutamate is capable of producing the highest maximum initial velocity for L-methionine production from 2-oxo-4-methylthiobutanoate, it is 5-10fold poorer in terms of substrate specificity when compared with L-tyrosine, L-tryptophan, and L-phenylalanine |
Klebsiella pneumoniae ATCC 13883 |
L-methionine + 2-oxoglutarate |
- |
? |
| 2.6.1.88 | 2-oxo-4-methylthiobutanoate + L-glutamate |
- |
Mycobacterium tuberculosis |
L-methionine + ? |
- |
? |
| 2.6.1.88 | 2-oxo-4-methylthiobutanoate + L-isoleucine |
- |
Mycobacterium tuberculosis |
L-methionine + 2-oxo-methylvalerate |
- |
? |
| 2.6.1.88 | 2-oxo-4-methylthiobutanoate + L-leucine |
- |
Mycobacterium tuberculosis |
L-methionine + 2-oxo-isocaproate |
- |
r |
| 2.6.1.88 | 2-oxo-4-methylthiobutanoate + L-phenylalanine |
- |
Klebsiella pneumoniae |
L-methionine + 2-oxo-3-phenylpropanoate |
- |
? |
